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6D1X

N-Domain Of Grp94, with the Charged Domain, In Complex With the Novel Ligand N-Propyl Carboxyamido Adenosine

Replaces:  1U0Y
Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue PA7 A 401
ChainResidue
AASN107
AHOH519
AHOH527
AHOH533
AHOH549
AALA111
AASP149
AMET154
AASN162
ALEU163
AVAL197
APHE199
ATYR200

site_idAC2
Number of Residues7
Detailsbinding site for residue PG4 A 402
ChainResidue
ALEU117
ATHR121
ATHR212
AARG237
ATHR240
APG4403
AHOH573

site_idAC3
Number of Residues4
Detailsbinding site for residue PG4 A 403
ChainResidue
ALYS137
ATRP282
APG4402
AHOH562

site_idAC4
Number of Residues7
Detailsbinding site for residue PG4 A 404
ChainResidue
AASN83
ALYS87
ALYS87
AILE90
ASER227
AHOH564
AHOH574

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE
ChainResidueDetails
ATYR94-GLU103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V
ChainResidueDetails
AASN107

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V
ChainResidueDetails
AASP149
APHE199

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V
ChainResidueDetails
AASN162

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P14625
ChainResidueDetails
ALYS168

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0
ChainResidueDetails
ASER172

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000255
ChainResidueDetails
ATHR288

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255
ChainResidueDetails
ASER306

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN107
AASN217

221716

PDB entries from 2024-06-26

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